1. Volume 84, Issue 1, Pages 489-500 (January 2003)
19Å Solution Structure of the Filarial Nematode Immunomodulatory Protein, ES-62 
Claire J. Ackerman, Margaret M. Harnett, William Harnett, Sharon M. Kelly, Dmitri I. Svergun, Olwyn Byron 
Biophysical Journal 
Volume 84, Issue 1, Pages (January 2003)
DOI: /S (03)
Copyright © 2003 The Biophysical Society Terms and Conditions

2. Figure 1
Multiple alignment of the amino acid sequence of ES-62 with those of its six protein homologs (Table 1). The multiple alignment was generated using MULTALIN (Corpet, 1988). The BLOSUM 62 matrix was used with a gap weight of 12 and a gap length weight of 2. The consensus levels were 90% for high homology (red) and 50% for low homology (blue). Symbols are as follows: ! is I or V; $ is L or M; % is F or Y; # is any one of NDQEBZ. The secondary structure for ES-62 predicted by JPRED (Cuff et al., 1998; Cuff and Barton, 1999) is shown beneath the alignment. Red cylinders represent α-helices and yellow arrows represent β-strands. In places helices appear broken reflecting the gaps inserted in the ES-62 sequence during alignment with its homologs. Boxed residues are those within ES-62 that are 32% identical with residues 74–168 of a leucyl aminopeptidase from Aeromonas proteolytica (PDB code, 1AMP).
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

3. Figure 2
Circular dichroism spectrum for tetrameric ES-62 at 0.33mg ml−1 in 91.5mM Na2HPO4, 58.5mM NaH2PO4, pH 7.0 buffer in a 0.02cm pathlength quartz cell. The data were best fit with 40% α-helix, 16% β-sheet, and 16% β-turn.
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

4. Figure 3
Theoretical scattering curves for the four proteins, PDB codes 1B0P (solid line), 1CX8 (dashed line), 1FCE (dotted line), and 1QJ2 (dashed-and-dotted line), predicted to share a high degree of secondary structure homology with ES-62. The curves were calculated from the coordinates of the homologous region of the proteins using the software CRYSOL (Svergun et al., 1995). The homologous regions of 1B0P and 1CX8 have similar solution shapes; 1QJ2 is slightly different and 1FCE is very different.
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

5. Figure 4
Mw,app plotted as a function of ES-62 monomer loading concentration from sedimentation equilibria obtained at rotor speeds of 8k rpm (●) and 10k rpm (○). The molecular weights of ES-62 monomer, dimer, and tetramer are indicated by arrows annotated m, d, and t, respectively.
Biophysical Journal  , DOI: ( /S (03) )
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6. Figure 5
A representative fit of the dimer-tetramer model to the sedimentation equilibrium primary data. The residuals of the fit are shown in the top panel.
Biophysical Journal  , DOI: ( /S (03) )
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7. Figure 6
Dissociation constant (Kd) (obtained from fitting the dimer-tetramer model to each of the sedimentation equilibrium primary data sets) plotted as a function of ES-62 monomer loading concentration and rotor speed, 8k rpm (●); 10k rpm (○).
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

8. Figure 7
Sedimentation coefficient as a function of ES-62 monomer loading concentration. The infinite dilution sedimentation coefficient obtained by extrapolation of these data to zero concentration is 9.85±0.25 S.
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

9. Figure 8
Composite experimental scattering pattern from ES-62 (●, with error bars), shape-scattering curve (○) and the scattering curve from the ab initio restored model (— —).
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions

10. Figure 9
Orthogonal views (top to bottom) of the low-resolution dummy atom model of ES-62 restored assuming point symmetries of (left to right) 1, 2, or 222.
Biophysical Journal  , DOI: ( /S (03) )
Copyright © 2003 The Biophysical Society Terms and Conditions